Viomycin sulfate

Viomycin sulfate

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Viomycin sulfate
Category Antibiotics
Catalog number BBF-03470
CAS 37883-00-4
Molecular Weight 783.77
Molecular Formula C25H43N13O10.H2O4S

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Description

It is a peptide antibiotic produced by the strain of Str. puniceus 1314-5 and Str. floridae A5014. It has broad-spectrum antibacterial and strong anti-mycobacterium effect. 1-10 μg/mL of Viomycin can inhibit the growth of most tuberculosis bacilli, the main effect is to inhibit the protein synthesis of bacteria, but bacteria are prone to develop drug resistance. In clinical application, it is only used as a second-line drug to treat tuberculosis.

Specification

Related CAS 32988-50-4 (free base)
Synonyms Tuberactinomycin B sulfate salt; celicomycin-sulfate; florimycin sulfate; Vinacetin A sulfate; hexanamide, 3,6-diamino-N-[(3S,6Z,9S,12S,15S)-6-[[(aminocarbonyl)amino]methylene]-3-[(4R,6S)-2-amino-3,4,5,6-tetrahydro-6-hydroxy-4-pyrimidinyl]-9,12-bis(hydroxymethyl)-2,5,8,11,14-pentaoxo-1,4,7,10,13-pentaazacyclohexadec-15-yl]-, (3S)-, sulfate (1:1) (salt)
Storage Store at 2-8°C
IUPAC Name (3S)-3,6-diamino-N-[(3S,6Z,9S,12S,15S)-3-[(4R,6S)-2-amino-6-hydroxy-1,4,5,6-tetrahydropyrimidin-4-yl]-6-[(carbamoylamino)methylidene]-9,12-bis(hydroxymethyl)-2,5,8,11,14-pentaoxo-1,4,7,10,13-pentazacyclohexadec-15-yl]hexanamide;sulfuric acid
Canonical SMILES C1C(N=C(NC1O)N)C2C(=O)NCC(C(=O)NC(C(=O)NC(C(=O)NC(=CNC(=O)N)C(=O)N2)CO)CO)NC(=O)CC(CCCN)N.OS(=O)(=O)O
InChI InChI=1S/C25H43N13O10.H2O4S/c26-3-1-2-10(27)4-16(41)32-12-6-30-23(47)18(11-5-17(42)37-24(28)36-11)38-20(44)13(7-31-25(29)48)33-21(45)14(8-39)35-22(46)15(9-40)34-19(12)43;1-5(2,3)4/h7,10-12,14-15,17-18,39-40,42H,1-6,8-9,26-27H2,(H,30,47)(H,32,41)(H,33,45)(H,34,43)(H,35,46)(H,38,44)(H3,28,36,37)(H3,29,31,48);(H2,1,2,3,4)/b13-7-;/t10-,11+,12-,14-,15-,17-,18-;/m0./s1
InChI Key AQONYROJHRNYQQ-QMAPKBLTSA-N

Properties

Appearance White Crystalline Powder
Antibiotic Activity Spectrum Mycobacteria
Melting Point 266°C (dec.)
Solubility Soluble in Methanol, Water

Reference Reading

1. Quantitative structure-activity relationships, molecular docking and molecular dynamics simulations reveal drug repurposing candidates as potent SARS-CoV-2 main protease inhibitors
Anacleto Silva de Souza, Robson Francisco de Souza, Cristiane Rodrigues Guzzo J Biomol Struct Dyn. 2022;40(21):11339-11356. doi: 10.1080/07391102.2021.1958700. Epub 2021 Aug 9.
The current outbreak of COVID-19 is leading an unprecedented scientific effort focusing on targeting SARS-CoV-2 proteins critical for its viral replication. Herein, we performed high-throughput virtual screening of more than eleven thousand FDA-approved drugs using backpropagation-based artificial neural networks (q2LOO = 0.60, r2 = 0.80 and r2pred = 0.91), partial-least-square (PLS) regression (q2LOO = 0.83, r2 = 0.62 and r2pred = 0.70) and sequential minimal optimization (SMO) regression (q2LOO = 0.70, r2 = 0.80 and r2pred = 0.89). We simulated the stability of Acarbose-derived hexasaccharide, Naratriptan, Peramivir, Dihydrostreptomycin, Enviomycin, Rolitetracycline, Viomycin, Angiotensin II, Angiotensin 1-7, Angiotensinamide, Fenoterol, Zanamivir, Laninamivir and Laninamivir octanoate with 3CLpro by 100 ns and calculated binding free energy using molecular mechanics combined with Poisson-Boltzmann surface area (MM-PBSA). Our QSAR models and molecular dynamics data suggest that seven repurposed-drug candidates such as Acarbose-derived Hexasaccharide, Angiotensinamide, Dihydrostreptomycin, Enviomycin, Fenoterol, Naratriptan and Viomycin are potential SARS-CoV-2 main protease inhibitors. In addition, our QSAR models and molecular dynamics simulations revealed that His41, Asn142, Cys145, Glu166 and Gln189 are potential pharmacophoric centers for 3CLpro inhibitors. Glu166 is a potential pharmacophore for drug design and inhibitors that interact with this residue may be critical to avoid dimerization of 3CLpro. Our results will contribute to future investigations of novel chemical scaffolds and the discovery of novel hits in high-throughput screening as potential anti-SARS-CoV-2 properties.Communicated by Ramaswamy H. Sarma.
2. Streptomycin potency is dependent on MscL channel expression
Irene Iscla, Robin Wray, Shuguang Wei, Bruce Posner, Paul Blount Nat Commun. 2014 Sep 10;5:4891. doi: 10.1038/ncomms5891.
The antibiotic streptomycin is widely used in the treatment of microbial infections. The primary mechanism of action is inhibition of translation by binding to the ribosome, but how it enters the bacterial cell is unclear. Early in the study of this antibiotic, a mysterious streptomycin-induced potassium efflux preceding any decrease in viability was observed; it was speculated that this changed the electrochemical gradient such that streptomycin better accessed the cytoplasm. Here we use a high-throughput screen to search for compounds targeting the mechanosensitive channel of large conductance (MscL) and find dihydrostreptomycin among the 'hits'. Furthermore, we find that MscL is not only necessary for the previously described streptomycin-induced potassium efflux, but also directly increases MscL activity in electrophysiological studies. The data suggest that gating MscL is a novel mode of action of dihydrostreptomycin, and that MscL's large pore may provide a mechanism for cell entry.

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